Histidinol dehydrogenase
     (HDH)
     (EC 1.1.1.23)
Histidinol-phosphate aminotransferase
     (EC 2.6.1.9)
     (Imidazole acetol-phosphate transaminase)

Gene name

	Name:	hisCD
	Synonyms:	hisD
	OrderedLocusNames:	plu1569

From

Photorhabdus luminescens subsp. laumondii

[TaxID: 141679]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Photorhabdus.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TT01;
DOI=10.1038/nbt886; PubMed=14528314 [NCBI, ExPASy, EBI, Israel, Japan]
Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.;
"The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens.";
Nat. Biotechnol. 21:1307-1313(2003).

Comments

FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine (By similarity).
CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
CATALYTIC ACTIVITY: L-histidinol + 2 NAD⁺ = L-histidine + 2 NADH.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
COFACTOR: Pyridoxal phosphate (By similarity).
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9 .
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9 .
SUBUNIT: Homodimer (By similarity).
SIMILARITY: In the N-terminal section; belongs to the histidinol dehydrogenase family.
SIMILARITY: In the C-terminal section; belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BX571864; CAE13862.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_928860.1; -.

3D structure databases

SMR

Q7N6I1; 5-432.

ModBase

Q7N6I1.

Enzyme and pathway databases

BioCyc

PLUM243265:PLU1569-MON; -.

Organism-specific databases

PhotoList

plu1569; -.

Ontologies

GO:0004399;	Molecular function: histidinol dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0004400;	Molecular function: histidinol-phosphate transaminase activity (inferred from electronic annotation from HAMAP).
GO:0000105;	Biological process: histidine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01023; fused; 1.
MF_01024; fused; 1.
PBIL [Tree]

InterPro

IPR004839; Aminotrans_I/II.
IPR001917; Aminotrans_II_pyridoxalP_BS.
IPR005861; HisP_aminotrans.
IPR001692; Histidinol_DHase.
IPR012131; Hstdl_DHase_prok.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.

PANTHER

PTHR21256:SF2; Hstdl_DH_prok; 1.

Pfam

PF00155; Aminotran_1_2; 1.
PF00815; Histidinol_dh; 1.
Pfam graphical view of domain structure.

PRINTS

PR00083; HOLDHDRGNASE.

ProDom

PD002680; Histidinol_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01141; hisC; 1.
TIGR00069; hisD; 1.

PROSITE

PS00599; AA_TRANSFER_CLASS_2; 1.
PS00611; HISOL_DEHYDROGENASE; 1.

Genome annotation databases

GeneID

2801564; -.

GenomeReviews

BX470251_GR; plu1569.

KEGG

plu:plu1569; -.

NMPDR

fig|243265.1.peg.1484; -.

Phylogenomic databases

HOGENOM

Q7N6I1; -.

Genome annotation databases

CMR

Q7N6I1; plu1569.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Aminotransferase; Complete proteome; Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Pyridoxal phosphate; Transferase; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 807`	`807`	`Putative histidine biosynthesis bifunctional protein hisCD.`	`PRO_0000153415`
`REGION`	`1 440`	`440`	`Histidinol dehydrogenase.`
`REGION`	`441 807`	`367`	`Histidinol-phosphate aminotransferase.`
`ACT_SITE`	`328 328`		`By similarity.`
`ACT_SITE`	`329 329`		`By similarity.`
`METAL`	`261 261`		`Zinc (By similarity).`
`METAL`	`264 264`		`Zinc (By similarity).`
`METAL`	`362 362`		`Zinc (By similarity).`
`METAL`	`421 421`		`Zinc (By similarity).`
`BINDING`	`655 655`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 807 AA [This is the length of the unprocessed precursor]

Molecular weight: 88850 Da [This is the MW of the unprocessed precursor]

CRC64: 648F98DD2F9F706E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTDHFDTLIR WQECHDEQQN ALLTRPAISA SVEISRTVEQ ILHAVKEYGD HTLREFSRRF 

        70         80         90        100        110        120 
DKTVIENIRI SPEEIAAAEN SLNNDIKQAM QQAMNNIRVF HEAQKPIKIE VETQPGVYCQ 

       130        140        150        160        170        180 
QVTRPIDSVG LYIPGGSAPL LSTVLMLGTP AQIAGCHKVV LCSPPPIANE ILYAATLCGI 

       190        200        210        220        230        240 
TEIFQIGGAQ AIAAMAFGTE SVPKVDKIFG PGNAYVTEAK RQVSQRVDGA TIDMPAGPSE 

       250        260        270        280        290        300 
LLIIADAGAN PVFVAADLLS QAEHGPDSQV ILVTPDEALA KKVITEIEKQ LTRLPRNQIA 

       310        320        330        340        350        360 
AKALAHSRII VTTSLQQCVE ISNRYGPEHL IIQTRQPEQL VEKITSAGSV FLGDWSPESA 

       370        380        390        400        410        420 
GDYASGTNHV LPTYGYTSTY SSLGLADFLK RMTIQQLTPQ GLLNLSQTIE TLAQAEQLTA 

       430        440        450        460        470        480 
HKNALTLRVA ALNIAGQGVN MNNIFDANLL ARENIRKLTP YMSARRLGGK GDVWLNANEY 

       490        500        510        520        530        540 
PLAPDFQCTE QTLNRYPDCQ PASVIRRYAA YAGLQPEQVL ACRGADESIE LLIRVFCEPG 

       550        560        570        580        590        600 
QDVVLFCPPT YGMYSVSAET FGVEQKKITA LENWQLDIEA IENNLDRVKL IYICSPNNPT 

       610        620        630        640        650        660 
GNAINPDSLR KILELTANRA IVTIDEAYIE FCPENSIASW LKNYPNLVIL RTLSKAFALA 

       670        680        690        700        710        720 
GLRCGFTLAS VDIITLLLKV IAPYPLSTPV ADIAAQALTA ENIAIMQKRV VEIRENRNDL 

       730        740        750        760        770        780 
QQALNKLAIV EKVFPSETNY ILVKFYDAET VFKTLWHQGI ILRDQRKQPG LEGCLRITIG 

       790        800 
SRKECERVVE AISALSTVNE QPKEIAN

Q7N6I1 in FASTA format

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View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools